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glycoprotein
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glycoprotein
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the activation peptide contains four potential N-linked glycosylation sites at Asn22, Asn51, Asn63 and Asn96. The 36000 catalytic unit of 309 amino acids is not glycosylated. The glycosylation of the activation peptide may act to stabilize and increase the half-life of circulating TAFI
glycoprotein
5 N-glycosylation sites at Asn22, Asn51, Asn63, Asn86, and Asn219, detailed carbohydrate analysis, overview, no O-glycosylation
glycoprotein
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different glycosylation patterns dependent on the enzyme source
glycoprotein
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the enzyme contains 4 potential N-glycosylation sites at Asn22, Asn51, Asn63, and Asn96, carbohydrates account for 20% of total mass of TAFI and are responsable for stabilization
proteolytic modification
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carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
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carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
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elastase can activate pro-carboxypeptidase R directly or indirectly through activation of some proteases
proteolytic modification
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the proenzyme has a MW of 55000 Da (401 aa), the enzyme has a MW of 35999 Da (309 aa), activated at proteolytis at Arg92
proteolytic modification
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the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of throbin is 0.74 per s, the Km-value is 0.00067 mM
proteolytic modification
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the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of throbin is 1.06 per s, the Km-value is 0.00084 mM
proteolytic modification
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the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of thrombin is 0.74 per s, the Km-value is 0.00082 mM
proteolytic modification
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the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of thrombin is 0.85 per s, the Km-value is 0.00083 mM
proteolytic modification
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activation of TAFI to TAFIa by cleavage through thrombin, activation reaction kinetics with wild-type isozymes and mutant enzymes at 37°C and pH 7.4
proteolytic modification
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activation pathways overview, cleavage of the activation peptide from proCPU, in vitro catalyzed through thrombin, meizothrombin, plasmin, trypsin, or neutrophil elastase, only the thrombin cleaved enzyme is active, in vivo by the thrombin/thrombomodulin complex in a Ca2+-dependent manner, kinetics, overview, the plasminogen activation system, overview
proteolytic modification
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Ca2+-dependent activation by thrombin at room temperature
proteolytic modification
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Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide
proteolytic modification
Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide, in vitro activation by trypsin at 37°C and pH 7.5
proteolytic modification
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ProCPU is activated by thrombin
proteolytic modification
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ProCPU is activated by thrombin or plasmin, the reaction is highly enhanced by thrombomodulin and glycosaminoglycans
proteolytic modification
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the enzyme is activated by thrombin
proteolytic modification
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the enzyme is synthesized as procarboxypeptidase B, activation through cleavage results in the active carboxypeptidase B and in the activation peptide of procarboxypeptidase B, enzyme activation is icreased in patients with acute pancreatitis, quantitative analysis of healthy persons' and patients' serum content of activation peptide, overview
proteolytic modification
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the enzyme is synthesized as zymogen TAFI, activation by the thrombin/thrombomodulin or by plasmin to the active form TAFIa, cleavage patterns, overview
proteolytic modification
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the enzyme is synthesized as zymogen, activation by the thrombin/thrombomodulin complex
proteolytic modification
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the enzyme is synthesized as zymogen, activation by the thrombin/thrombomodulin complex or by plasmin
proteolytic modification
the enzyme is synthesized as zymogen, activation by thrombin and thrombomodulin at pH 8.5
proteolytic modification
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the enzyme is synthesized as zymogen, activation of TAFI by thrombin to TAFIa, inactivation of TAFIa by cleavage through thrombin at Arg302
proteolytic modification
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the inactive zymogen proCPU is Ca2+-dependently activated by thrombin/thrombumodulin or plasmin
proteolytic modification
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the proenzyme is activated by many factors including thrombin, thrombomodulin, plasmmin, and trypsin
proteolytic modification
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the recombinant pre-enzyme and pre-enzyme chimera are activated by thrombin/thrombomodulin in presence of Ca2+ through cleavage at Arg92 releasing the activation peptide, cleavage of Arg302 leads to inactivation by disruption of the active site, cleavage pattern with wild-type and chimeric muatnt enzymes, overview, plasmin activates inactive TAFI and inactivates active TAFI, overview
proteolytic modification
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proteolytic enzymes activate TAFI into TAFIa, by cleaving off the N-terminal activation peptide (amino acids 1-92), from the enzyme moiety. TAFIa is active both before and after removal of the activation peptide, and the half-life of TAFIa is identical in the two preparations
proteolytic modification
the inactive precursor procarboxypeptidase U is converted to its active form by thrombin, the thrombin-thrombomodulin complex or plasmin
proteolytic modification
the plasma zymogen pro-carboxypeptidase R is a plasma zymogen activated during coagulation
proteolytic modification
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the enzyme is synthesized as zymogen TAFI, activation by the thrombin to the active form TAFIa
proteolytic modification
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the enzyme is synthesized as zymogen, activation of TAFI by thrombin to TAFIa, inactivation of TAFIa by cleavage through thrombin at Arg302
proteolytic modification
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carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
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carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
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procarboxypeptidase R is generated from pro-carboxypeptidase R, a plasma zymogen, by proteolytic enzymes such as thrombin, thrombin-thrombomodulin complex and plasmin
proteolytic modification
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the enzyme is activated by thrombin